PJB-2025-415
Binding Dynamics of Banana Lectin with L-fucose: Integrative Spectroscopic, Crystallographic, and in Silico Studies
Rida Arif1
Abstract
Banana lectin (Banlec) is a dimeric plant lectin with glucose/mannose specificity and is also capable of recognizing other carbohydrates. Therefore, the present study was conducted to evaluate the binding modalities of Banlec with L-fucose. Banlec was purified from Musa paradisiaca, and its binding with L-fucose was analyzed via different biophysical techniques. In the first step, the binding affinity of Banlec with L-fucose was analyzed via UV-Vis spectroscopic analysis, which revealed a decreased absorption intensity at 280 nm with increasing concentrations of L-fucose. Thermodynamic parameters, such as binding constant Kb= (4.78 ± 0.08) ×104 M-1, dissociation constant (Kd=21.8 ± 0.3 µM), and Gibbs free energy (ΔG°=-26.7 kJ mol-1), suggested a favourable interaction. Results of circular dichroism spectroscopic (CD) analysis showed that binding of fucose did not alter the secondary structure of Banlec. Differential scanning fluorimetry showed a slight increase in melting temperature (ΔTm = +0.5 °C) upon L-fucose binding. Additionally, X-ray crystal structure of the Banlec–fucose complex was resolved at 2.95 Å. Two molecules of L-fucose showed binding with Ser33, Gly34, His63, His84, and Gly105 amino acid residues. Molecular docking studies further supported the experimental findings. Hence, this study provides structural insights into the carbohydrate-binding features of Banlec, particularly its interaction with L-fucose.
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